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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Protein and Amino Acids, 1999 Pp. 19-75. Washington, D.C. National Academy Press 1 Committee Overview INTRODUCTION Proteins form the major constituents of muscle, catalyze virtually all chemical reactions in the body, regulate gene expression, and comprise the major structural elements of all cells. Individual amino acids, the components of proteins, also serve as neurotransmitters, hormones, and modulators of various physiological processes. Every aspect of physiology involves proteins. According to Bier (see Chapter 5), credit for the name "protein" is given to the Dutch chemist Gerardus Johannes Mulder, who wrote an article in French that was published in a Dutch journal on July 30, 1838. In this article, he asserted that this material was the essential general principle of all animal body constituents and defined it by the Greek word proteus (which he translated to the Latin, primarius, meaning primary). Mulder appears to have taken this word directly from a letter sent to him by the Swedish chemist Jacques Bursailleus on July 10, 1838, in which the name protein had been suggested. Aside from the amazing fact of a Dutch chemist borrowing n Latin word from a Swedish
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance chemist, which he defined in Greek in an article written in French for a Dutch journal, the entire sequence of events appears to have occurred in a period of 20 days, demonstrating the efficiency of both mail service and scientific publication in those days. The relationship between dietary protein and bodily protein metabolism is a major focus of research today. Many questions remain regarding the validity of methods for assessing protein balance; thus, the question of how best to assess dietary protein requirements remains unanswered. In addition, the influence of genetics, hormones, physical activity, infectious processes, and environmental stresses on protein metabolism and protein requirements continues to be explored. Another major focus of research that is of great interest is the role of dietary protein and amine acids in modulating physiological function, as measured for example by physical and mental performance. The possibility that protein or individual amine acids in quantities that exceed those required to maintain protein balance may have the potential to contribute to performance optimization is of great interest. THE ARMY'S INTEREST IN DIETARY PROTEIN AND PROTEIN BALANCE Because of the unique demands placed on soldiers in combat, the military is particularly concerned about the role that dietary protein may play in controlling muscle mass and strength; response to injury, infection, and environmental stress; and cognitive performance. As described in Chapter 3 by Karl Friedl, the longer, more isolated deployments and maneuvers that are becoming more commonplace may limit access to rations. The nutritional studies of Ranger trainees conducted by the U.S. Army Research Institute of Environmental Medicine (USARIEM) (IOM, 1992, 1993b) identified losses of up to 30 percent in lean body mass (including organs, such as the liver, plasma, and proteins) after 3 weeks of limited food intake and high energy expenditure. Although increased energy intake offset these losses somewhat, they were still significant, suggesting the need for additional energy, protein, or both. In these studies, the observed decrease in lean body mass was accompanied by changes in serum levels of several hormones including testosterone, insulin-like growth factor I (IGF-I), and triiodothyronine (T3) (Friedl, 1997; Nindl et al., 1997), the significance of which is unclear. Because the administration of these hormones is known to stimulate protein synthesis under some conditions, the Army maintains considerable interest in exploring their potential both to ameliorate the losses in lean body mass sustained by troops under conditions of extreme negative energy balance and to stimulate an increase in muscle mass and physical performance. In contrast to the limited intakes of protein and energy measured in the Ranger studies, a more recent study, in which soldiers subsisted on the field ration known as Meals, Ready to Eat (MREs) for 30 days, showed
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance average energy intakes of 2500 kcal/d and protein intakes of 103 g/d (Thomas et al., 1995), raising questions about the optimum protein-to-energy ratio for performance and health. As the typical battlefield scenario becomes more automated, soldiers must attend to increasing numbers of signals in the face of increasing amounts and sources of noise, with increasingly dangerous consequences for failure. Thus, the possibility that cognitive performance may depend on diet and that performance optimization may be achievable through dietary modifications such as amino acid supplements is of considerable interest to the military. A 1994 report by the Committee on Military Nutrition Research (CMNR), entitled Food Components to Enhance Performance, briefly considered the influence of protein and amino acids (and all other dietary components) on physical and cognitive performance and response to stress (IOM, 1994). Data were presented on the effect of protein-to-carbohydrate ratio on mental alertness, the effect of physical activity on protein requirements, and the influence of branched-chain amino acids, tyrosine, and tryptophan in pharmacological amounts on cognitive function. The report concluded that the potential ability of tyrosine supplements to sustain alertness and cognitive performance in the face of environmental stress merited further investigation. Finally, the risk of injury and infection faced by soldiers in the field is extremely high. At the same time, conditions of sleep and food deprivation, environmental extremes, and heightened emotional stress all exert a negative impact on the immune system. The CMNR report Military Strategies for Sustainment of Nutrition and Immune Function in the Field (IOM, 1999), considered the effects of diet, including protein and individual amino acids such as glutamine, on immune response and concluded that although the role of energy intake in immune function is probably more significant than that of protein, individual amino acids such as glutamine and arginine appear to play crucial roles in modulating immune function. The effects of these amino acids are considered in greater detail in this report. ESTIMATION OF PROTEIN REQUIREMENTS Current estimates of protein requirements for mature humans and the methods used to assess these requirements are being scrutinized by the research community and are a source of considerable disagreement. Protein Metabolism The requirement for protein arises from growth, from the need to replace obligatory losses, and from the need to respond to environmental stimuli. The
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance FIGURE 1-1 Pathways of protein turnover. Source: Young and Marchini, 1990. breakdown products of protein—amino acids—enter the free amino acid pool of the body (distributed among body fluids and tissues) from four sources: (1) dietary proteins; (2) so-called dispensable (nonessential) amino acids, which can be synthesized in the body; (3) breakdown products of body protein (particularly skeletal muscle, the largest tissue in the body and the site of protein storage); and (4) the products of recycling by intestinal microbes (Figure 1-1). In mature humans, a homeostatic mechanism maintains the balance between tissue protein synthesis and breakdown by drawing on the free amino acid pool. Methods for Assessment of Protein Requirements Because the majority of nitrogen in the body is associated with protein and amino acids, nitrogen has been used as a marker for assessing whole-body and tissue protein flux and status. The traditional method for assessing whole-body protein metabolism is nitrogen balance, where nitrogen (N) intake and output (in feces, sweat, and urine, as well as other miscellaneous sources) are measured and the difference [Nbal=(Nin = Nout)] is expressed in grams of nitrogen per day (g N/d). Total body protein loss or retention is then calculated using the conversion factor of 6.25 g N/g protein (Munro and Crim, 1994). A state of positive nitrogen balance exists when the total nitrogen output is less than the total nitrogen ingested. Positive nitrogen balance requires adequate protein and energy intake plus a stimulus for synthesis. A state of positive nitrogen balance (an anabolic state) exists for the synthesis of new tissues during the growth observed in childhood, adolescence, and pregnancy. When dietary protein or energy intake is inadequate or an individual experiences an acute-
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance phase response, nitrogen excretion exceeds nitrogen intake and a state of negative nitrogen balance exists (net protein catabolism). When dietary protein is adequate or more than adequate and energy intake matches energy output, a state of nitrogen equilibrium exists (Nin = Nout for any intake above the required level). A state of nitrogen equilibrium is required to maintain total body protein mass. Altering protein or energy intake or physical activity may alter nitrogen balance. Despite the usefulness of nitrogen balance assessment in estimating the adequacy of protein intake, there are significant limitations to its use, including overestimation of nitrogen intake and incomplete collections of urine, feces, or sweat, which result in an underestimation of nitrogen output. The net outcome is an overestimate of nitrogen retention and of the body's ability to adapt to inadequate protein intakes; these overestimates limit the ability of the nitrogen balance technique to assess nitrogen requirement. The limitations of nitrogen balance assessment are discussed further below and by Millward and Young in Chapters 9 and 10, respectively. In the mid-1940s, stable isotopes of hydrogen (2H) and nitrogen (15 N), were made available for use in biomedical research. However, the mass spectrometry technology that would use these isotopes for rapid analysis of biological specimens was not widely available until the late 1970s. With the improvement of this technology and the widespread availability of stable isotope-labeled metabolites, amino acid kinetic studies have come to augment nitrogen balance in examining the effects of dietary protein, energy, and physical activity on overall protein metabolism. Amino acids labeled with stable isotopes of hydrogen (2H), nitrogen (15N), and carbon (13C) have been administered orally and intravenously. With the use of the primed continuous infusion technique, amino acid turnover can be studied in subjects of all ages under many physiological conditions (Munro and Crim, 1994). The calculation of amino acid flux (Q) is based on the following assumptions: (1) the body's flee amino acid pool is a homogeneous mixture that can be sampled from the plasma pool; (2) the only sources of the target amino acids entering the body pool are dietary protein (I) and intracellular protein breakdown (B); and (3) amino acid removal from this pool occurs by irreversible oxidation (E) or synthesis into protein (Z). In reality, a large quantity of recycled amino acids is derived daily from the breakdown of body proteins. In addition to the sizable turnover of blood cells, mucosal cells of gastric and intestinal villi are continuously moved toward villus tips where they slough off and undergo digestion; released free amino acids are then reabsorbed into the plasma pool (Munro and Crim, 1994). Thus, the equation Q = B + I = E + Z describes the steady-state relationship in which the total entry of amino acids into the free amino acid pool (B + I) is equal to the total exit of amino acids from the free amino acid pool (E + Z). Rates of protein synthesis and protein breakdown can be calculated from this equation (Picou and Taylor-
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance Roberts, 1969). At isotopic steady state, total amine acid turnover (Q) is measured, and the rate of protein breakdown can be calculated knowing the rate of amine acid intake. Likewise, the rate of protein synthesis can be calculated when the rate of amine acid disappearance is known. If a 13C-labeled amine acid is used, oxidation can be measured from 13CO2 excretion rates. Because of its unique role as an amine acid that is oxidized in skeletal muscle and not converted to a tricarboxylic acid (TCA) cycle intermediate, leucine (in the 13C form) has been the amine acid of choice for many amine acid kinetic studies. However, due to its unique metabolism, it may not be representative of the entire pool of amine acids. Glycine labeled with 15N has also been used extensively to study protein synthesis and breakdown because it has the advantage of ubiquitous utilization. FAO/WHO/UNU Requirements and RDAs: Current Estimates of Average Protein Intake Estimations of protein and amine acid requirements are currently based on nitrogen balance studies. The 1985 report of the Food and Agriculture Organization (FAO), World Health Organization (WHO), and United Nations University (UNU) proposed a protein requirement of 0.625 g per kilogram of body weight per day (g/kg BW/d) for egg or beef protein and a ''safe" level of 0.75 g/kg BW/d for mixed protein if the protein is as digestible as egg or beef (FAO/WHO/UNU, 1985). The current recommended dietary allowance (RDA) for protein in the U.S. diet (which is derived by adding two standard deviations to the estimated requirement) is 0.8 g/kg BW/d for adult men and women (Table 1-1) (NRC, 1989). Also based on nitrogen balance data, the recommendation for total essential or indispensable amine acids (IAAs) as a percentage of protein intake is 43 percent for infants and 11 percent for adults (FAO/WHO/UNU, 1985). Essential (indispensable) and nonessential (dispensable) amine acids are traditionally distinguished on a nutritional basis because essential amine acids cannot be synthesized by the body and must be part of the diet to permit growth or to maintain nitrogen balance, whereas nonessential amine acids can be synthesized by the body. Metabolically, however, the distinctions are less clear because a number of essential amine acids can be formed by transamination (at least in laboratory animals). By this criterion, only the amine acids lysine and threonine appear not to be synthesized by transamination and are therefore indispensable (as discussed further below, the concentrations of these two amine acids in cereal proteins are so low as to limit their ability to sustain growth). By this same argument, glutamic acid and serine are the only truly dispensable amine acids because they can be synthesized by reductive amination of ketoacids. A
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance TABLE 1-1 Recommended Dietary Allowances for Protein Age (years) or Condition Weight (kg) RDA g/d RDAg/kg BW/d Males 19-24 72 58 0.8 25-50 79 63 0.8 51+ 77 63 0.8 Females 19-24 58 46 0.8 25-50 63 50 0.8 51+ 65 50 0.8 Pregnant 60 Lactating (first 6 months) 65 Lactating (second 6 months) 62 SOURCE: Adapted from NRC (1989). third class—the conditionally essential amino acids—is synthesized from other amino acids. However, this synthesis is confined to particular organs and may be limited by certain physiological factors such as age or disease state (Reeds and Becket, 1996). As knowledge increases and techniques improve, the distinction between essential and nonessential amino acids becomes less clear. Adding to this lack of clarity are observations such as the one by Stucky and Harper (1962), who found that if rats were fed a diet adequate in nitrogen but lacking in nonessential amino acids, the growth rate of the animals was significantly decreased. Importance of the Debate over Indispensable Amino Acid Requirements Although consensus exists at present for the adult protein requirement this is not the case for the adult requirement of indispensable amino acids. Since the 1985 FAO/WHO/UNU report, Young and coworkers have presented data that contradict the findings of the report; based on these data, Young suggests that the adult requirement for total IAAs is 31 percent of the protein requirement, or about three times the FAO/WHO/UNU estimate (McLarney et al., 1996; Young, 1987, 1994; Young and El-Khoury, 1995a; Young and Marchini, 1990; Young et al., 1989; see also Chapter 10). This contention of the group at Massachusetts Institute of Technology (MIT) for higher indispensable amino acid needs has been countered by Millward and colleagues (Millward, 1994; Millward and Rivers, 1988, 1989; see also Chapter 9), who find significant methodological problems in the studies of Young and coworkers. This debate is important, because it influences whether or not protein quality is an issue to be considered
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance in setting protein requirements. Protein quality, a measure of the efficiency with which dietary protein is utilized, can be assessed by comparison of the amine acid profile of a given protein to various amine acid scoring patterns such those developed by the FAO/WHO for various age groups. If the requirement for IAAs is low (as proposed by FAO/WHO and Millward), the pattern is easily matched by most proteins, and protein quality ceases to be an issue in setting protein requirements for adults. However, if the FAO estimates are incorrect and indispensable amine acids are required in the higher amounts proposed by Young, individual protein sources may duplicate the scoring patterns poorly, and protein quality may then become a significant determinant of protein requirements. Argument for Higher Indispensable Amine Acid Requirements Young has based his argument for higher indispensable amine acid requirements on two related measures: the obligatory oxidative losses of these amine acids and the calculated obligatory losses based on daily nitrogen loss. In the latter calculation, Young assumes that the efficiency of dietary protein use is about 70 percent and that the lost protein has the composition of mixed body protein. Indispensable amine acid requirements calculated in these two ways (the MIT pattern) are approximately the same. In 1991, an expert panel of FAO/WHO also agreed that the IAA needs for adults are greater than those in the 1985 report and proposed that the amine acid pattern for preschool children (FAO/WHO, 1991), a pattern similar to the MIT pattern, be recommended for adults. Young argues that protein and indispensable amine acid intakes have to be high enough to provide sufficient flux for optimum "metabolic control." This concept proposes that a high flux rate of amine acids or other substrates provides a kinetic basis for a sensitive control mechanism to ensure adequate provision of metabolic intermediates. In the case of protein, these important intermediates would be amine acids such as glutamine, tyrosine, and tryptophan, which have important physiological roles to play independent of their incorporation into protein. To prove their point, Young and colleagues carried out a long-term study to compare the effects of the FAO (FAO/WHO/UNU, 1985), MIT, and egg patterns of indispensable amine acids on amine acid balance in healthy young adults (Marchini et al., 1993). After a week on the egg pattern (high in IAAs), 20 young men were placed on diets resembling either the FAO, the MIT, or the egg pattern for three weeks. Based on a negative leucine balance while the subjects were on the FAO (compared with the MIT) pattern and changes in serum amine acid profiles, Marchini et al. (1993) concluded that the FAO pattern is not capable of maintaining amine acid homeostasis. Since the 1991 FAO/WHO meeting, several groups have reevaluated the existing data and concluded that the original FAO recommendations were likely
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance to be underestimates but stopped short of endorsing the MIT pattern (Fuller and Garlick, 1994; Waterlow, 1996). In 1994, an expert panel met to consider the issue. After the meeting, the panel recommended that the entire question of how amino acid requirements are determined be reexamined but that, in the interim, the MIT pattern be accepted (Clugston et al., 1996). However, as subsequently pointed out by Millward and Waterlow (1996), this recommendation was not the consensus of the attendees but was inserted during postmeeting editing. Argument Against Higher Indispensable Amino Acid Requirements Millward and colleagues have challenged Young's data point by point (Millward, 1994; Millward and Rivers, 1988, 1989; see also Chapter 9). They suggest first that Young's stable isotope amino acid oxidation data, derived from stable isotope-labeled amino acid infusion studies, are flawed for two reasons. First, the amount of tracer used in the infusion studies is itself high enough to influence the oxidation of the amino acid and thus the balance determined. Second, the enrichment of the amino acid precursors being oxidized is not accurately measured, a critical issue in the interpretation of stable isotope research. Next, Millward argues that there is no valid basis for assuming that the obligatory amino acid losses (as calculated from obligatory nitrogen loss) resemble the pattern of body protein, because some of the amino acids released during normal turnover are known to be preferentially recycled (lysine and threonine). In addition, he believes that the metabolic demand for IAAs is determined not by the need for high flux rates, but by the obligatory losses and the relative ability of the body to adapt on a diurnal basis to varying levels of these amino acids in the diet (he notes that digestive enzymes secreted in response to a meal can, over the short run, assist in meeting the indispensable amino acid needs by breaking down themselves). Finally, Millward points out that in the longer-term study mentioned above (Marchini et al., 1993), nitrogen balance did not differ significantly between the MIT and the FAO patterns; this finding suggests that both patterns support overall body protein economy. The Rebuttal Young agrees with Millward that there are inherent difficulties in defining requirements for indispensable amino acids. The two most serious and difficult-to-resolve problems are (1) accounting for the mass of stable isotope infused, which is large enough to affect nitrogen balance, and (2) determining the true precursor enrichment rate of the amino acid being infused and under study. On the first point, the agreement between IAA requirements calculated from oxidation rates and from nitrogen balance leads Young to conclude that the
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance mass of stable isotope infused does not "profoundly" affect the calculation of amine acid oxidation rates. He agrees, however, that this issue deserves more attention. On the question of true precursor amine acid enrichments in the stable isotope experiments, Young points out that this is a problem primarily for lysine since measurements in experiments with branched-chain amine acids are made from keto acids derived intracellularly from the infused amine acid. Studies using L-[l-13C]phenylalanine as an indicator amine acid for determining the lysine requirement have yielded a requirement of 40 mg/kg BW/d (Duncan et al.; 1996, Zello et al., 1993), an estimate close to Young's own tentative new requirement for lysine (50 mg/kg BW/d). In this technique, the indicator amine acid (labeled phenylalanine) is infused at graded levels of lysine intake, and the "breakpoint" in 13CO2 excretion is measured, under the assumption that the uptake of phenylalanine into protein will be sharply decreased and its oxidation sharply increased at the point where lysine intake becomes inadequate. Young's definition of the maintenance amine acid pattern for adults is generally similar to the amine acid pattern in body protein, except for lysine, threonine, and methionine, whose patterns were derived more from the results of his tracer studies. Young agrees that the body has significant ability to conserve lysine under conditions of inadequate intake. His calculations suggest that the lysine requirement is 30 percent lower than that found in mixed body protein, due to lysine conservation that results from diurnal cycling. Resolution of the Debate The practical implications of the debate between Young and Millward revolve primarily around lysine: the lysine content of cereal proteins is limiting for growth. If Millward is correct, then all dietary proteins, whether plant or animal, contain enough lysine and other amine acids to support adequate protein nutriture of adults if consumed in amounts that meet the protein requirement (although some military personnel in the 18-22-year age group are still growing, a factor that might influence the requirement for some amine acids). Millward has shown that wheat protein, a protein that is particularly low in lysine, is well utilized in adults in the postprandial period, even when net protein synthesis occurs. He suggests that the low level of lysine in this protein is supplemented by the tissue free amine acid pools. However, older data from Longenecker (Longenecker, 1961, 1963; Longenecker and Hause, 1959, 1961) show that the ingestion of wheat protein by dogs or humans may result in decreased plasma lysine levels accompanied by increased levels of other indispensable amine acids. Such data support the contention that a postprandial breakdown of body protein may supply the indispensable amine acids necessary for synthesis. However, under such circumstances, other IAAs may be used less efficiently for protein synthesis when lysine is limiting in the protein consumed,
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The Role of Protein and Amino Acids in Sustaining and Enhancing Performance which supports Young's belief that the indispensable amino acid requirement is higher than currently recommended. Thus, the controversy over requirements for IAAs is still unresolved. The implications of this debate for the current state of knowledge of protein and amino acid requirements for the military depend in part on the current intake of dietary protein and amino acids by military personnel and in part on other factors influencing protein requirements in these individuals, as discussed below. STRESSORS THAT INFLUENCE PROTEIN REQUIREMENTS As discussed by Friedl in Chapter 3, the stressors encountered most frequently by military personnel are high levels of physical activity with Or without energy restriction; illness, injury, and infection; and environmental extremes. Although each of these stressors may somehow influence protein metabolism and protein requirements directly, they also produce changes in hormonal status that can influence protein metabolism as well. The impact of each of these factors on protein metabolism and requirements has been the subject of intense investigation in the civilian research community. A brief summary of relevant findings is presented here. Physical Activity and Energy Restriction The question of whether individuals who routinely engage in intensely physical occupational or athletic activities have increased requirements for dietary protein appears to have arisen from the observations that during exercise, muscle protein is utilized for fuel and that exercise can lead to an increase in muscle mass. However, whether protein requirements are in fact increased by physical activity is unclear and a subject of intense controversy. In Chapter 11, Rennie reviews the role of protein and its breakdown products, amino acids, in exercising muscle and discusses changes in protein metabolism induced by energy deficit. Exercise and Amino Acid Catabolism A major function of amino acid breakdown in muscle during periods of exercise is to supply tricarboxylic acid intermediates (anaplerosis) so that the oxidation of acetyl coenzyme A (CoA) can proceed at rates appropriate to the energy needs of the contractile apparatus. The exercise-induced increase in muscle alanine production may be a marker for this process. Specifically, glutamate can react with pyruvate, via the action of alanine-aminotransferase, to produce alanine and α-ketoglutarate. The latter then feeds into the TCA cycle,
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Representative terms from entire chapter: